ID A0A554VGK6_9FLAO Unreviewed; 802 AA.
AC A0A554VGK6;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=HAD-IC family P-type ATPase {ECO:0000313|EMBL:TSE06531.1};
GN ORFNames=FOF46_18870 {ECO:0000313|EMBL:TSE06531.1};
OS Aquimarina algiphila.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Aquimarina.
OX NCBI_TaxID=2047982 {ECO:0000313|EMBL:TSE06531.1, ECO:0000313|Proteomes:UP000318833};
RN [1] {ECO:0000313|EMBL:TSE06531.1, ECO:0000313|Proteomes:UP000318833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M91 {ECO:0000313|EMBL:TSE06531.1,
RC ECO:0000313|Proteomes:UP000318833};
RA Meng X.;
RT "The draft genome sequence of Aquimarina algiphila M91.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TSE06531.1}.
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DR EMBL; VLNR01000044; TSE06531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A554VGK6; -.
DR OrthoDB; 1521937at2; -.
DR Proteomes; UP000318833; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR021993; ATPase-cat-bd.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR Pfam; PF12156; ATPase-cat_bd; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000318833};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..282
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 424..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 766..792
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..150
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 802 AA; 90483 MW; E8CB9D2E424BE694 CRC64;
MSESTCFHCG IDCGKTVIKF DQKTFCCNGC KTVYDIFSSN DLSCYYDLQS APGAIPKEIQ
GKYDYLDTDI IAKKLIEFDD GNTQIITLYI PHIHCSSCIW ILENLHKLQT AITASQVNFP
KKTVRITFKS DAISLKEVVI LLHTIGYEPY ISLDDYASAK KKIDRSLLYK LGIAGFAFGN
VMFLSFPEYF EVSEYWLEQY KPIFRWLMFA FSIPVVFYAA QEYFISAYKG LRSKLLNIDV
PIALGILVLF LRSTAEIIFD WGTGFFDSLT GLVFFLLLGK FFQKKTYSFL SFERDYKSYF
PIAVTRISTA KHKKERKEEN IQIYDIKKGD RLLIRNGELI PVDAILIDGN AQIDYSFVTG
ESDSVHKQSG DTLFAGGRQL YGAIEIEVLK SVEQSYLTQL WSNDVFNTDK LASFTNLTDI
ISKYFTIAIL CIAIISTSYW LFTDVSKAIH VFTAVLIIAC PCALALARPF ALGNILRIFG
KNKFYLKNAD VIERLALTDT IIFDKTGTIT TTITSNVTYE GMQLTPEEES LLKNTLRASN
HPLSRTLYNV LAEHDILTLD EYQEYVGKGI EGKSADHTIK IGSPNFVGNE DLSKVFSTTV
HVSTNDEYKG HYTFHNQYRN GVKKVFNQLF KNYQLAILSG DNEGEKEYLQ KVLPENTSLI
FNQKPDDKLN YIKMLQQQHK KVIMVGDGLN DAGALAQSDV GIAVSENVNV FSPACDGILD
ASRFDKISTY LMISKNAIKI IKSSFILSFL YNCVGLYFAV TGQLSPIIAA ILMPLSSISI
IVYVTILTNW IGQKVNDNHK DL
//